A novel function for proSAAS as an amyloid anti-aggregant in Alzheimer's disease. - Wikidata - wikimedia - TriplyDB

A novel function for proSAAS as an amyloid anti-aggregant in Alzheimer's disease.

A novel function for proSAAS as an amyloid anti-aggregant in Alzheimer's disease.

http://www.wikidata.org/entity/Q37625372

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Chaperones in Neurodegeneration Pax6 Inactivation in the Adult Pancreas Reveals Ghrelin as Endocrine Cell Maturation Marker The neural chaperone proSAAS blocks α-synuclein fibrillation and neurotoxicity.Current pharmacotherapy and putative disease-modifying therapy for Alzheimer's disease.PCSK1 Variants and Human Obesity.Label-free quantitative comparison of cerebrospinal fluid glycoproteins and endogenous peptides in subjects with Alzheimer's disease, mild cognitive impairment, and healthy individuals.7B2 chaperone knockout in APP model mice results in reduced plaque burden.

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A novel function for proSAAS as an amyloid anti-aggregant in Alzheimer's disease.

http://www.wikidata.org/entity/Q37625372

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on 24 October 2013

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

A novel function for proSAAS as an amyloid anti-aggregant in Alzheimer's disease.

@en

A novel function for proSAAS as an amyloid anti-aggregant in Alzheimer's disease.

@nl

type

label

A novel function for proSAAS as an amyloid anti-aggregant in Alzheimer's disease.

@en

A novel function for proSAAS as an amyloid anti-aggregant in Alzheimer's disease.

@nl

prefLabel

A novel function for proSAAS as an amyloid anti-aggregant in Alzheimer's disease.

@en

A novel function for proSAAS as an amyloid anti-aggregant in Alzheimer's disease.

@nl

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P1433

Journal of Neurochemistry

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A novel function for proSAAS as an amyloid anti-aggregant in Alzheimer's disease.

@en

P2093

Akina Hoshino

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Casey Berridge

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Iris Lindberg

http://www.w3.org/2001/XMLSchema#string

Michael Helwig

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Sina Rezaei

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P2860

Identification and characterization of proSAAS, a granin-like neuroendocrine peptide precursor that inhibits prohormone processing

The extracellular chaperone clusterin influences amyloid formation and toxicity by interacting with prefibrillar structures

RAGE-mediated signaling contributes to intraneuronal transport of amyloid-beta and neuronal dysfunction

7B2 is a neuroendocrine chaperone that transiently interacts with prohormone convertase PC2 in the secretory pathway

Synapse loss and microglial activation precede tangles in a P301S tauopathy mouse model

Mutant presenilins specifically elevate the levels of the 42 residue beta-amyloid peptide in vivo: evidence for augmentation of a 42-specific gamma secretase

The neuroendocrine protein 7B2 suppresses the aggregation of neurodegenerative disease-related proteins

Processing of proSAAS in neuroendocrine cell lines

Peptide fingerprinting of Alzheimer's disease in cerebrospinal fluid: identification and prospective evaluation of new synaptic biomarkers

Proinsulin processing in the diabetic Goto-Kakizaki rat

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419-430

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scholarly article

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10.1111/JNC.12454

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3

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128

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Jason L. Eriksen

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2013-10-24T00:00:00Z

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257532120

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24102330

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Alzheimer's disease

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3946950

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